The unfolded protein response plays dual roles in rice stripe virus infection through fine-tuning the movement protein accumulation.

The unfolded protein response plays dual roles in rice stripe virus infection through fine-tuning the movement protein accumulation.
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未折叠蛋白反应通过微调运动蛋白积累在水稻条纹病毒感染中发挥双重作用

DOI:
10.1371/journal.ppat.1009370
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发表时间:
2021-03
期刊:
影响因子:
6.7
通讯作者:
Zhou X
Zhou X
中科院分区:
医学1区
文献类型:
--
作者:
Li C;Xu Y;Fu S;Liu Y;Li Z;Zhang T;Wu J;Zhou X

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植物病毒的运动是一个复杂的过程,需要病毒编码的运动蛋白和多种宿主因子的支持。未折叠蛋白反应(UPR)在植物病毒侵染过程中发挥重要作用,但UPR如何调控病毒侵染尚不清楚。在这里,我们发现水稻条纹病毒(RSV)在烟叶中引发UPR。rsv诱导的UPR激活宿主自噬途径,rsv编码的运动蛋白NSvc4是自噬降解的目标。作为一种抵消,我们发现NSvc4劫持了upr激活的i型j结构域蛋白NbMIP1s,以保护自己免受自噬降解。出乎意料的是,我们发现NbMIP1以非规范的不依赖于hsp70的方式稳定NSvc4。在benthamiana中沉默NbMIP1家族基因可延缓RSV感染,而过表达nbmip14 b可促进病毒细胞间运动。此外,水稻NbMIP1家族的同源物OsDjA5也以类似的方式促进RSV感染。本研究举例说明了RSV和宿主植物之间的军备竞赛,并通过微调病毒运动蛋白的积累揭示了UPR在RSV感染中的双重作用。
The movement of plant viruses is a complex process that requires support by the virus-encoded movement protein and multiple host factors. The unfolded protein response (UPR) plays important roles in plant virus infection, while how UPR regulates viral infection remains to be elucidated. Here, we show that rice stripe virus (RSV) elicits the UPR in Nicotiana benthamiana. The RSV-induced UPR activates the host autophagy pathway by which the RSV-encoded movement protein, NSvc4, is targeted for autophagic degradation. As a counteract, we revealed that NSvc4 hijacks UPR-activated type-I J-domain proteins, NbMIP1s, to protect itself from autophagic degradation. Unexpectedly, we found NbMIP1 stabilizes NSvc4 in a non-canonical HSP70-independent manner. Silencing NbMIP1 family genes in N. benthamiana, delays RSV infection, while over-expressing NbMIP1.4b promotes viral cell-to-cell movement. Moreover, OsDjA5, the homologue of NbMIP1 family in rice, behaves in a similar manner toward facilitating RSV infection. This study exemplifies an arms race between RSV and the host plant, and reveals the dual roles of the UPR in RSV infection though fine-tuning the accumulation of viral movement protein.
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